Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Mouse complement component C4 is devoid of classical pathway C5 convertase subunit activity

R O Ebanks1, D E Isenman

  • 1Department of Biochemistry, University of Toronto, Ontario, Canada.

Molecular Immunology
|February 1, 1996
PubMed
Summary

Mouse complement C4 exhibits low hemolytic activity due to a lack of classical pathway C5 convertase subunit activity. This deficiency is linked to sequence differences in the beta-chain, impacting C5 binding and alternative pathway reliance.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Molecular characterization and quantitative analysis of superoxide dismutases in virulent and avirulent strains of Aeromonas salmonicida subsp. salmonicida.

Journal of bacteriology·2003
Same author

Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21).

Journal of immunology (Baltimore, Md. : 1950)·2000
Same author

Two clusters of acidic amino acids near the NH2 terminus of complement component C4 alpha'-chain are important for C2 binding.

Journal of immunology (Baltimore, Md. : 1950)·2000
Same author

Identification of residues within the 727-767 segment of human complement component C3 important for its interaction with factor H and with complement receptor 1 (CR1, CD35).

The Journal of biological chemistry·1999
Same author

The covalent binding reaction of complement component C3.

Journal of immunology (Baltimore, Md. : 1950)·1998
Same author

X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2.

Science (New York, N.Y.)·1998

Area of Science:

  • Immunology
  • Complement System Biology

Background:

  • Mouse complement C4 (C4) shows lower hemolytic activity than other mammals.
  • Previous studies attributed this to technical issues or species incompatibilities.

Purpose of the Study:

  • Investigate if sequence differences in mouse C4's beta-chain affect its C5 convertase subunit activity.
  • Determine the cause of mouse C4's low hemolytic activity.

Main Methods:

  • Utilized a multi-step hemolytic assay dependent on classical pathway C5 cleavage.
  • Ruled out species incompatibilities between mouse C4 and guinea pig C5.
  • Analyzed the role of specific beta-chain residues in C5 binding and convertase activity.

Main Results:

  • Mouse C4 is completely deficient in classical pathway C5 convertase subunit activity.

Related Experiment Videos

  • The low hemolytic activity of mouse C4 is solely due to alternative pathway C5 convertase.
  • Human C4 residues 455-469 are crucial for C5 binding; substitutions in mouse C4 compromise this function.

    • Conclusions:

    • Sequence differences in the mouse C4 beta-chain, particularly residues 455-469, abolish classical pathway C5 convertase activity.
    • Mouse C4's hemolytic activity relies on the alternative pathway, not the classical pathway.
    • Other non-conserved regions likely contribute to C5 binding in human C4.